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Search results 1 to 2 out of 2 for Sgf29

Category restricted to ProteinDomain (x)

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Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: SAGA-associated factor 29 (SGF29) is a chromatin reader and a component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK [, ]. In the SAGA complex, SGF29 binds histone H3 that has been methylated at Lys-4 (H3K4me), and preferably binds the trimethylated form (H3K4me3) []. SGF29 also acts as a boundary, preventing the spread of heterochromatin into neighbouring genes [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].
Protein Domain
Type: Domain
Description: SAGA-associated factor 29 (SGF29) is involved in transcriptional regulation as a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes [, , , , ]. SGF29 specifically recognises and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for the trimethylated form (H3K4me3). It also may be involved in MYC-mediated oncogenic transformation [].This entry represents a the two tandem tudor-like domains found at the C-terminal of yeast and human SAGA-associated factor 29 proteins and the plant homologues. Each of them has a negatively-charged pocket capable of binding H3A1 and an aromatic cage for the recognition of H3K4me2/3 residues [, ].